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Human and plant proteins as reservoirs of host defence peptides

Human and plant proteins as reservoirs of host defence peptidesaf Andrea Bosso
Bag om Human and plant proteins as reservoirs of host defence peptides

Antimicrobial peptides (AMPs), known also as host defense peptides (HDPs), are fundamental evolutionarily conserved components of innate immunity. Constitutively or inducibly expressed in response to invasion by pathogens, they operate synergistically with other defence molecules to combat infections. Despite differences in their size and sequence, many of them share a net positive charge at neutral pH, and fold into amphipathic structures, often after contact with bacterial surfaces. HDPs are attractive alternative candidates for antibiotic treatment, because they offer several advantages over the currently used drugs. They combat pathogens by targeting bacterial membranes, thus impairing essential membrane-related functions, and, in some cases, also target intracellular components. Due to their peculiar mechanism, the resistance towards these peptides would be difficult for the bacteria to develop. As described in this book, several proteins, including proteins apparently not involved in immunity, can behave as sources of HDPs hidden in their primary structures and released by the action of host and/or bacterial proteases.

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  • Sprog:
  • Engelsk
  • ISBN:
  • 9786202087445
  • Indbinding:
  • Paperback
  • Sideantal:
  • 104
  • Udgivet:
  • 17. juni 2019
  • Størrelse:
  • 150x7x220 mm.
  • Vægt:
  • 173 g.
  • 2-3 uger.
  • 16. december 2024
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Beskrivelse af Human and plant proteins as reservoirs of host defence peptides

Antimicrobial peptides (AMPs), known also as host defense peptides (HDPs), are fundamental evolutionarily conserved components of innate immunity. Constitutively or inducibly expressed in response to invasion by pathogens, they operate synergistically with other defence molecules to combat infections. Despite differences in their size and sequence, many of them share a net positive charge at neutral pH, and fold into amphipathic structures, often after contact with bacterial surfaces. HDPs are attractive alternative candidates for antibiotic treatment, because they offer several advantages over the currently used drugs. They combat pathogens by targeting bacterial membranes, thus impairing essential membrane-related functions, and, in some cases, also target intracellular components. Due to their peculiar mechanism, the resistance towards these peptides would be difficult for the bacteria to develop. As described in this book, several proteins, including proteins apparently not involved in immunity, can behave as sources of HDPs hidden in their primary structures and released by the action of host and/or bacterial proteases.

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